Basic salivary proline-rich protein 3 precursor

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Q04118 (PRB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Basic salivary proline-rich protein 3

Alternative name(s):
Parotid salivary glycoprotein G1
Proline-rich protein G1

Gene names

Name:

PRB3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a receptor for the Gram-negative bacterium F.nucleatum. Ref.4
Subunit structure	The Gl-8 variant forms a disulfide-bonded heterodimer with salivary perodixase.
Subcellular location	Secreted.
Post-translational modification	The Gl-8 variant contains an interchain disulfide bond with salivary peroxidase. N- and O-glycosylated; contains about 50% carbohydrate. This is composed of highly fucosylated N-linked saccharides, the major structure is a biantennary asialosaccharide containing 2 fucose residues on one antenna and an unsubstituted terminal lactosamine sequence on the other. The Gram-negative bacterium F.nucleatum binds to carbohydrates containing unsubstituted GalBeta1,4GlcNAc residues. Ref.4 Ref.6 Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P₃ position is mostly lysine. The endoprotease may be of microbial origin. Besides on the N-terminal of mature PRB3, pyroglutamate formation found on at least Gln-67, Gln-88, Gln-214 and Gln-295. Ref.5
Polymorphism	The number of repeats is polymorphic and varies among different alleles. The sequence shown is that of allele L (long). There is an allele S (short) which contains 6 tandem repeats.
Sequence caution	The sequence CAA30477.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
PTM	Disulfide bond Glycoprotein Phosphoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	extracellular region Non-traceable author statement Ref.4. Source: UniProtKB
Molecular function	Gram-negative bacterial cell surface binding Non-traceable author statement Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

Potential

Chain

17 – 309

293

Basic salivary proline-rich protein 3

PRO_0000022097

Regions

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Region

210

10 X 21 AA tandem repeats of [RH]-P-G-K-P-[EQ]-G-[PQS]-P-[PS]-Q-[GE]-G-N-[QK]-[SP]-[QR]-[GR]-P-P-P

Compositional bias

36 – 308

273

Pro-rich

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid

Modified residue

Phosphoserine Ref.6

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...); prevelant in head and neck cancer patients Ref.6

Glycosylation

O-linked (Hex) Ref.6

Glycosylation

108

N-linked (GlcNAc...) Potential

Glycosylation

129

N-linked (GlcNAc...) Potential

Glycosylation

150

N-linked (GlcNAc...) Potential

Glycosylation

171

N-linked (GlcNAc...) Potential

Glycosylation

192

N-linked (GlcNAc...) Potential

Glycosylation

213

N-linked (GlcNAc...) Potential

Glycosylation

255

N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant

P → C in Gl-8; requires 2 nucleotide substitutions. Ref.3

VAR_019696

Natural variant

158 – 220

Missing in allele S.

VAR_055031

Natural variant

186

P → Q. Ref.2
Corresponds to variant rs11054208 [ dbSNP | Ensembl ].

VAR_055032

Experimental info

Sequence conflict

R → P in CAA30728. Ref.1

Sequence conflict

47 – 53

PQRTPPP → SQGPPPR in CAA30728. Ref.1

Sequence conflict

P → S in CAA30477. Ref.1

Sequence conflict

R → P in CAA30728. Ref.1

Sequence conflict

P → Q in CAA30728. Ref.1

Sequence conflict

102

Q → P in CAA30728. Ref.1

Sequence conflict

119

K → E in CAA30728. Ref.1

Sequence conflict

137

R → H in CAA30728. Ref.1

Sequence conflict

158

H → R in CAA30728. Ref.1

Sequence conflict

158

H → R in AAH96211. Ref.2

Sequence conflict

237

Q → R in CAA30728. Ref.1

Sequence conflict

264

G → R in CAA30728. Ref.1

Sequence conflict

264

G → R in CAA30477. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q04118 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: A8FCBEBA784618C6
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FASTA

309

30,980

        10         20         30         40         50         60 
MLLILLSVAL LALSSAQSLN EDVSQEESPS VISGKPEGRR PQGGNQPQRT PPPPGKPEGR 

        70         80         90        100        110        120 
PPQGGNQSQG PPPRPGKPEG PPPQGGNQSQ GPPPRPGKPE GQPPQGGNQS QGPPPRPGKP 

       130        140        150        160        170        180 
EGPPPQGGNQ SQGPPPRPGK PEGPPPQGGN QSQGPPPHPG KPEGPPPQGG NQSQGPPPRP 

       190        200        210        220        230        240 
GKPEGPPPQG GNQSQGPPPR PGKPEGPPPQ GGNQSQGPPP RPGKPEGSPS QGGNKPQGPP 

       250        260        270        280        290        300 
PHPGKPQGPP PQEGNKPQRP PPPGRPQGPP PPGGNPQQPL PPPAGKPQGP PPPPQGGRPH 


RPPQGQPPQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Length polymorphisms in human proline-rich protein genes generated by intragenic unequal crossing over." Lyons K.M., Stein J.H., Smithies O. Genetics 120:267-278(1988) [PubMed: 2851479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES L AND S), POLYMORPHISM.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE L), VARIANT GLN-186.
[3]	"Alleles at the PRB3 locus coding for a disulfide-bonded human salivary proline-rich glycoprotein (Gl 8) and a null in an Ashkenazi Jew." Azen E.A., Minaguchi K., Latreille P., Kim H.-S. Am. J. Hum. Genet. 47:686-697(1990) [PubMed: 2171329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-309 (ALLELE S), VARIANT GL-8 CYS-53, INTERACTION WITH SALIVARY PEROXIDASE, DISULFIDE BOND.
[4]	"Structure and bacterial receptor activity of a human salivary proline-rich glycoprotein." Gillece-Castro B.L., Prakobphol A., Burlingame A.L., Leffler H., Fisher S.J. J. Biol. Chem. 266:17358-17368(1991) [PubMed: 1894623] [Abstract] Cited for: PROTEIN SEQUENCE OF 68-92; 110-127; 131-148; 173-190 AND 194-211, FUNCTION, GLYCOSYLATION. Tissue: Saliva.
[5]	"Identification of Lys-Pro-Gln as a novel cleavage site specificity of saliva-associated proteases." Helmerhorst E.J., Sun X., Salih E., Oppenheim F.G. J. Biol. Chem. 283:19957-19966(2008) [PubMed: 18463091] [Abstract] Cited for: PROTEOLYTIC PROCESSING, MASS SPECTROMETRY.
[6]	"Finding new posttranslational modifications in salivary proline-rich proteins." Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C., Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L. Proteomics 10:3732-3742(2010) [PubMed: 20879038] [Abstract] Cited for: GLYCOSYLATION AT ASN-87; SER-89 AND ASN-255, PYROGLUTAMATE FORMATION AT GLN-17, PHOSPHORYLATION AT SER-24, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07637 Genomic DNA. Translation: CAA30477.1. Sequence problems. X07881 Genomic DNA. Translation: CAA30728.1. BC096209 mRNA. Translation: AAH96209.1. BC096210 mRNA. Translation: AAH96210.1. BC096211 mRNA. Translation: AAH96211.1.
IPI	IPI00006699.
PIR	A36298. B36298. S10889.
RefSeq	NP_006240.4. NM_006249.4.
UniGene	Hs.73031.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q04118.
Polymorphism databases
DMDM	229462763.
Proteomic databases
PRIDE	Q04118.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381842; ENSP00000371264; ENSG00000197870.
GeneID	5544.
KEGG	hsa:5544.
Organism-specific databases
CTD	5544.
GeneCards	GC12M011418.
H-InvDB	HIX0201930.
HGNC	HGNC:9339. PRB3.
MIM	168840. gene.
neXtProt	NX_Q04118.
PharmGKB	PA33701.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00540000070914.
Gene expression databases
ArrayExpress	Q04118.
Bgee	Q04118.
CleanEx	HS_PRB3.
Genevestigator	Q04118.
GermOnline	ENSG00000197870. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

PRB3_HUMAN

Accession

Primary (citable) accession number: Q04118
Secondary accession number(s): Q15188

Q9UCT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	May 5, 2009
Last modified:	January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents